Drosophila chaoptin, a member of the leucine-rich repeat family, is a photoreceptor cell-specific adhesion molecule

EMBO J. 1990 Jun;9(6):1969-77.


Drosophila chaoptin, required for photoreceptor cell morphogenesis, is a member of the leucine-rich repeat family of proteins. On the basis of biochemical and genetic analyses we previously proposed that chaoptin might function as a cell adhesion molecule. To test this hypothesis, chaoptin cDNA driven by the hsp 70 promoter was transfected into non-self-adherent Drosophila Schneider line 2 (S2) cells. Following heat shock induction of chaoptin expression, the transfected S2 cells formed multicellular aggregates. Mixing experiments of chaoptin expressing and non-expressing cells suggest that chaoptin expressing cells adhere homotypically. Previously it was shown that chaoptin is exclusively localized to photoreceptor cells. Thus, chaoptin is a cell-type-specific adhesion molecule. Biochemical analyses presented in this paper demonstrate that chaoptin is linked to the extracellular surface of the plasma membrane by covalent attachment to glycosyl-phosphatidylinositol. We propose that chaoptin and several other members of the leucine-rich repeat family of proteins define a new class of cell adhesion molecules.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Adhesion
  • Cell Aggregation / drug effects
  • Cell Membrane / metabolism
  • Cells, Cultured
  • DNA / genetics
  • Drosophila / genetics*
  • Drosophila / ultrastructure
  • Drosophila Proteins
  • Glycolipids / physiology
  • Leucine / genetics
  • Membrane Glycoproteins / genetics*
  • Membrane Glycoproteins / immunology
  • Multigene Family*
  • Photoreceptor Cells / metabolism*
  • Sensitivity and Specificity
  • Time Factors
  • Type C Phospholipases / pharmacology


  • Drosophila Proteins
  • Glycolipids
  • Membrane Glycoproteins
  • chp protein, Drosophila
  • DNA
  • Type C Phospholipases
  • Leucine